GUDP_ECOLI
ID GUDP_ECOLI Reviewed; 450 AA.
AC Q46916; Q2MA45;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable galactarate/D-glucarate transporter GudP {ECO:0000305};
GN Name=gudP {ECO:0000303|PubMed:10762278}; Synonyms=ygcZ;
GN OrderedLocusNames=b2789, JW2760;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP POSSIBLE FUNCTION.
RX PubMed=9772162; DOI=10.1021/bi981124f;
RA Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily:
RT characterization of the (D)-glucarate/galactarate catabolic pathway in
RT Escherichia coli.";
RL Biochemistry 37:14369-14375(1998).
RN [4]
RP POSSIBLE FUNCTION, INDUCTION, AND GENE NAME.
RX PubMed=10762278; DOI=10.1128/jb.182.9.2672-2674.2000;
RA Monterrubio R., Baldoma L., Obradors N., Aguilar J., Badia J.;
RT "A common regulator for the operons encoding the enzymes involved in D-
RT galactarate, D-glucarate, and D-glycerate utilization in Escherichia
RT coli.";
RL J. Bacteriol. 182:2672-2674(2000).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Probably involved in the uptake of galactarate and/or D-
CC glucarate (Probable). May also transport D-glycerate (Probable).
CC {ECO:0000305|PubMed:10762278, ECO:0000305|PubMed:9772162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactarate(in) + H(+)(in) = galactarate(out) + H(+)(out);
CC Xref=Rhea:RHEA:28478, ChEBI:CHEBI:15378, ChEBI:CHEBI:16537;
CC Evidence={ECO:0000305|PubMed:10762278, ECO:0000305|PubMed:9772162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucarate(in) + H(+)(in) = D-glucarate(out) + H(+)(out);
CC Xref=Rhea:RHEA:28474, ChEBI:CHEBI:15378, ChEBI:CHEBI:30612;
CC Evidence={ECO:0000305|PubMed:10762278, ECO:0000305|PubMed:9772162};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate(in) + H(+)(in) = (R)-glycerate(out) + H(+)(out);
CC Xref=Rhea:RHEA:70927, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659;
CC Evidence={ECO:0000305|PubMed:10762278};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced in the presence of D-galactarate, D-glucarate or D-
CC glycerate. {ECO:0000269|PubMed:10762278}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
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DR EMBL; U29581; AAB40439.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75831.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76861.1; -; Genomic_DNA.
DR PIR; A65061; A65061.
DR RefSeq; NP_417269.1; NC_000913.3.
DR RefSeq; WP_000097072.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46916; -.
DR SMR; Q46916; -.
DR BioGRID; 4263242; 17.
DR STRING; 511145.b2789; -.
DR PaxDb; Q46916; -.
DR PRIDE; Q46916; -.
DR EnsemblBacteria; AAC75831; AAC75831; b2789.
DR EnsemblBacteria; BAE76861; BAE76861; BAE76861.
DR GeneID; 947265; -.
DR KEGG; ecj:JW2760; -.
DR KEGG; eco:b2789; -.
DR PATRIC; fig|1411691.4.peg.3945; -.
DR EchoBASE; EB2961; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_5_1_6; -.
DR InParanoid; Q46916; -.
DR OMA; CINVLTY; -.
DR PhylomeDB; Q46916; -.
DR BioCyc; EcoCyc:B2789-MON; -.
DR BioCyc; MetaCyc:B2789-MON; -.
DR PRO; PR:Q46916; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042836; P:D-glucarate metabolic process; IEP:EcoCyc.
DR GO; GO:0019580; P:galactarate metabolic process; IEP:EcoCyc.
DR GO; GO:0015698; P:inorganic anion transport; IEA:GOC.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..450
FT /note="Probable galactarate/D-glucarate transporter GudP"
FT /id="PRO_0000121385"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..58
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..109
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..176
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..290
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..415
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 450 AA; 49142 MW; E0599FACCB1BB488 CRC64;
MSSLSQAASS VEKRTNARYW IVVMLFIVTS FNYGDRATLS IAGSEMAKDI GLDPVGMGYV
FSAFSWAYVI GQIPGGWLLD RFGSKRVYFW SIFIWSMFTL LQGFVDIFSG FGIIVALFTL
RFLVGLAEAP SFPGNSRIVA AWFPAQERGT AVSIFNSAQY FATVIFAPIM GWLTHEVGWS
HVFFFMGGLG IVISFIWLKV IHEPNQHPGV NKKELEYIAA GGALINMDQQ NTKVKVPFSV
KWGQIKQLLG SRMMIGVYIG QYCINALTYF FITWFPVYLV QARGMSILKA GFVASVPAVC
GFIGGVLGGI ISDWLMRRTG SLNIARKTPI VMGMLLSMVM VFCNYVNVEW MIIGFMALAF
FGKGIGALGW AVMADTAPKE ISGLSGGLFN MFGNISGIVT PIAIGYIVGT TGSFNGALIY
VGVHALIAVL SYLVLVGDIK RIELKPVAGQ
